The objective of this proposed research is to add to our understanding of the relationships between biosynthesis, conformation and physiological role of two proteins associated with certain cancers. One of the proteins, human lysozyme, is found in extraordinary amounts in urine of individuals with monocytic or monomyelocytic leukemia. The other is a human gamma-G myeloma immunoglobulin. In the case of the myeloma protein, the investigation is initially aimed at studying the specificity involved in chain assembly. Partial reduction and separation of reduced chains allow study of rates of reoxidation and recombination of heavy chains in the presence and absence of light chains. Light chains derived from other immunoglobulins will also be used in competition experiments. Conformational comparisons of separated and recombined chains may shed light on domain structures, role of disulfides, conformational aspects and reactivity of target immunoglobulins in lymphocytes. Human, rat and mouse lysozymes are investigated from the points of view of binding of inhibitor, enzyme specificity, acid-base properties, fluorescence, CD of aromatic side chains and related biophysico-chemical properties. Partial reduction and reoxidation experiments are intended to shed light on questions of the nature of conformational states available to the protein depending on conditions and influence of inhibitors and substrate on rates of achievement of enzymatically active states.